rdf:type |
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lifeskim:mentions |
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pubmed:issue |
23
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pubmed:dateCreated |
1992-1-9
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pubmed:databankReference |
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M72335,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M80723,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M80724,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M81661,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M81662,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M81664,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M81665,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M81666,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M82973,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S71210,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S71212
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pubmed:abstractText |
cDNA clones containing sequence similarity to the multifunctional vertebrate protein disulfide-isomerase (PDI, EC 5.3.4.1) were isolated from an alfalfa (Medicago sativa L.) cDNA library by screening with a cDNA sequence encoding human PDI. The polypeptide encoded by a clone designated B2 consisted of 512 amino acids and was characterized by a 24-amino acid hydrophobic leader sequence, two regions with absolute identity to the vertebrate PDI active site (Ala-Pro-Trp-Cys-Gly-His-Cys-Lys), and a C-terminal endoplasmic reticulum retention signal (Lys-Asp-Glu-Leu). The overall identity of the B2 sequence to that of human PDI was 35% at the amino acid level (79% when conservative substitutions were included) and 39% at the nucleotide level; this included homology between B2 and the region of human PDI believed to be involved in binding estrogens. The deduced amino acid sequence of B2 was also 35% identical to that of a rat form I phosphatidylinositol-specific phospholipase C. Lysates from Escherichia coli cells harboring an expression plasmid bearing the B2 sequence contained significantly elevated levels of PDI activity. Southern analysis indicated the presence of a small PDI-related gene family in alfalfa, of which B2 appeared to correspond to a single gene. An approximately 2-kilobase B2 transcript was expressed in all alfalfa organs tested. In alfalfa cell suspension cultures, B2 transcripts were strongly induced by tunicamycin but not by exposure to fungal elicitor.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-16667176,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-16667295,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-16667764,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-1840696,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-2002068,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-2025222,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-2254345,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-2295602,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-2344363,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-2351674,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-2441623,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-2458190,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-2544299,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-2558866,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-2668279,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-271968,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-2851999,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-3034602,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-3036064,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-3243435,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-3387233,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-3398923,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-3545499,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-3619939,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-3627262,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-3714490,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-3840230,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-3907854,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-6312838,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-7174650,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-903355,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-942051
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Isomerases,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Oligodeoxyribonucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol...,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoinositide Phospholipase C,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoric Diester Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Disulfide-Isomerases,
http://linkedlifedata.com/resource/pubmed/chemical/RNA
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0027-8424
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
88
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
10941-5
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pubmed:dateRevised |
2010-9-7
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pubmed:meshHeading |
pubmed-meshheading:1720555-Humans,
pubmed-meshheading:1720555-Animals,
pubmed-meshheading:1720555-Vertebrates,
pubmed-meshheading:1720555-Medicago sativa,
pubmed-meshheading:1720555-DNA,
pubmed-meshheading:1720555-Escherichia coli,
pubmed-meshheading:1720555-RNA,
pubmed-meshheading:1720555-Plant Proteins,
pubmed-meshheading:1720555-Isomerases,
pubmed-meshheading:1720555-Membrane Proteins,
pubmed-meshheading:1720555-Cells, Cultured,
pubmed-meshheading:1720555-Amino Acid Sequence,
pubmed-meshheading:1720555-Macromolecular Substances,
pubmed-meshheading:1720555-Binding Sites,
pubmed-meshheading:1720555-Molecular Sequence Data,
pubmed-meshheading:1720555-Transcription, Genetic,
pubmed-meshheading:1720555-Phosphoric Diester Hydrolases,
pubmed-meshheading:1720555-Cloning, Molecular,
pubmed-meshheading:1720555-Oligodeoxyribonucleotides,
pubmed-meshheading:1720555-Restriction Mapping,
pubmed-meshheading:1720555-Sequence Homology, Nucleic Acid
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